ORBi: Laurent Guy - Des-, syn- and anti-oxyimino-delta 3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine beta-lactamase and D-alanyl-D-alanine-cleaving serine and Zn2+-containing peptidases

Reference : Des-, syn- and anti-oxyimino-delta 3-cephalosporins. Intrinsic reactivity and reaction w...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology Life sciences : Microbiology
	To cite this reference:	http://hdl.handle.net/2268/83015

Title :	Des-, syn- and anti-oxyimino-delta 3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine beta-lactamase and D-alanyl-D-alanine-cleaving serine and Zn2+-containing peptidases
Language :	English
Author, co-author :	Laurent, Guy [Facultés Universitaires Notre-Dame de la Paix - Namur - FUNDP > Laboratoire de Chimie Moleculaire Structurale > > > >]
	Durant, François [Facultés Universitaires Notre-Dame de la Paix - Namur - FUNDP > Laboratoire de Chimie Moleculaire Structurale > > >]
	Frère, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
	Klein, Daniel [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Publication date :	15-Mar-1984
Journal title :	Biochemical Journal
Publisher :	Portland Press
Volume :	218
Issue/season :	3
Pages :	933-937
Audience :	International
ISSN :	0264-6021
e-ISSN :	1470-8728
City :	London
Country :	United Kingdom
Keywords :	[en] carboxypeptidases/antagonists & inhibitors ; cephalosporins ; chemical phenomena ; chemistry ; hydrolysis ; kinetics ; penicillinase ; serine-type d-ala-d-ala carboxypeptidase ; structure-activity relationship ; substrate specificity
Abstract :	[en] The presence and configuration (syn or anti) of an oxyimino group in the 7 (beta)-acyl side chain of 3-cephems do not modify the intrinsic reactivity of the beta-lactam ring, but have highly enzyme-specific effects. When compared with the corresponding desoxyimino beta-lactam compound: (i) with the plasmid-mediated Escherichia coli RTEM-2 serine beta-lactamase, the substrate activity of the anti isomer is increased and that of the syn isomer is decreased; (ii) with the Streptomyces R61 serine D-alanyl-D-alanine cleaving peptidase (a highly penicillin-sensitive enzyme), the rate of enzyme acylation is not or only little affected when the oxyimino group is in the syn configuration, but is decreased when the oxyimino group is in the anti configuration; (iii) with the Actinomadura R39 serine D-alanyl-D-alanine-cleaving peptidase (an exceedingly highly penicillin-sensitive enzyme), the rate of enzyme acylation is unaffected whatever the configuration of the substituent. The oxidation of the sulphur atom of the dihydrothiazine ring on the beta-face of the molecule makes it both a poorer inactivator of the DD-peptidases and a poorer substrate of the beta-lactamase. The Streptomyces albus G Zn2+-containing D-alanyl-D-alanine-cleaving peptidase (a highly penicillin-resistant enzyme) remains highly resistant to all compounds tested.
Funders :	Fonds de la Recherche Scientifique Médicale - FRSM
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/83015
	also: http://hdl.handle.net/2268/83040

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